Endoplasmic reticulum acyltransferase with prokaryotic substrate preference contributes to triacylglycerol assembly in <i>Chlamydomonas</i>
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- Yeongho Kim
- School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588;
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- Ee Leng Terng
- School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588;
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- Wayne R. Riekhof
- School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588;
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- Edgar B. Cahoon
- Center for Plant Science Innovation, University of Nebraska-Lincoln, Lincoln, NE 68588;
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- Heriberto Cerutti
- School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588;
説明
<jats:title>Significance</jats:title> <jats:p> The acyl chain composition of <jats:italic>Chlamydomonas</jats:italic> triacylglycerols (TAGs) suggests that they are assembled from prokaryotic precursors, proposed to be synthesized in the chloroplast. However, in most eukaryotes, the endoplasmic reticulum (ER) appears to be the main organelle for storage TAG biosynthesis. Interestingly, <jats:italic>Chlamydomonas reinhardtii</jats:italic> has a distinct lysophosphatidic acid acyltransferase that localizes to the ER but resembles prokaryotic lysophosphatidic acid acyltransferases (LPAATs) in its substrate preference. Thus, <jats:italic>Chlamydomonas</jats:italic> and related green algae, unlike land plants, can synthesize “prokaryotic” acyl-lipids in the ER, with intriguing implications for biotechnological applications. </jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 115 (7), 1652-1657, 2018-01-30
Proceedings of the National Academy of Sciences
